BMRB Entry 17131

Title:
NMR resonance assignment of the N-terminal domain of Latrodectus hesperus (black widow) major ampullate spider silk fibroin 1
Deposition date:
2010-08-16
Original release date:
2010-11-10
Authors:
Kessler, Horst; Hagn, Franz
Citation:

Citation: Hagn, Franz; Thamm, Christopher; Scheibel, Thomas; Kessler, Horst. "pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk--implications for fiber formation."  Angew. Chem. Int. Ed. Engl. 50, 310-313 (2011).

Assembly members:

Assembly members:
N1, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: black widow spider   Taxonomy ID: 256737   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Latrodectus hesperus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts458
15N chemical shifts131
1H chemical shifts496

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1N11

Entities:

Entity 1, N1 132 residues - Formula weight is not available

1   METGLYGLNALAASNTHRPROTRPSERSER
2   LYSALAASNALAASPALAPHEILEASNSER
3   PHEILESERALAALASERASNTHRGLYSER
4   PHESERGLNASPGLNMETGLUASPMETSER
5   LEUILEGLYASNTHRLEUMETALAALAMET
6   ASPASNMETGLYGLYARGILETHRPROSER
7   LYSLEUGLNALALEUASPMETALAPHEALA
8   SERSERVALALAGLUILEALAALASERGLU
9   GLYGLYASPLEUGLYVALTHRTHRASNALA
10   ILEALAASPALALEUTHRSERALAPHETYR
11   GLNTHRTHRGLYVALVALASNSERARGPHE
12   ILESERGLUILEARGSERLEUILEGLYMET
13   PHEALAGLNALASERALAASNASPVALTYR
14   ALASER

Samples:

sample_1: sodium phosphate 10 mM; sodium chloride 300 mM; H2O 95%; D2O 5%; N1, [U-99% 13C; U-99% 15N], 0.85 mM

sample_conditions_1: ionic strength: 0.32 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

SPARKY v3.115, Goddard - chemical shift assignment, data analysis

PASTA v1.1, Kessler and Gemmercker - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

GB ABR68856 ABR68857 ABY67402 ABY67406 ABY67410

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks